Evidence map›Paper›PMID 19325126›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

RBX1/ROC1 disruption results in early embryonic lethality due to proliferation failure, partially rescued by simultaneous loss of p27.

Mingjia Tan, Shannon W Davis, Thomas L Saunders, Yuan Zhu, Yi Sun

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.5field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

54 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Protein neddylation and its role in health and diseases.Signal transduction and targeted therapy · 2024
    Review
  5. Review
  6. The Cullin-RING Ligase Family in Immune Regulation.Advances in experimental medicine and biology · 2024
    Review
  7. Article
  8. Inactivation ofMedComm · 2023
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. LSD1 destabilizes FBXW7 and abrogates FBXW7 functions independent of its demethylase activity.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. Article
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Mingjia TanDivision of Radiation and Cancer Biology, Department of Radiation Oncology, University of Michigan Comprehensive Cancer Center, 4424B MS I, 1301 Catherine Street, Ann Arbor, MI 48109-5936, USA.
Shannon W Davis
Thomas L Saunders
Yuan Zhu
Yi Sun
University of Michigan–Ann Arbor · US

Funding

XenograftP30CA046592 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Scott Michael Schuetze · 1988 to 2026
$178.2M
SAG E3 ubiquitin ligase in regulation of transformation and carcinogenesisR01CA118762 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2006 to 2015
$2.6M
SAG E3 ubiquitin ligase in angiogenesis & carcinogenesisR01CA111554 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2005 to 2010
$1.8M
Substrates of SAG-SCF E3 ligase regulate hypoxia responseR21CA116982 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SUN, YI · 2006 to 2007
$313k
NCI NIH HHS CA111554NCI NIH HHS CA116982NCI NIH HHS CA118762NCI NIH HHS CA46592NCI NIH HHS P30 CA046592NCI NIH HHS R01 CA111554NCI NIH HHS R01 CA118762NCI NIH HHS R21 CA116982
6 · The paper itself

Abstract

RBX1 (RING box protein-1) or ROC1 (regulator of cullins-1) is the RING component of SCF (Skp1, Cullins, F-box proteins) E3 ubiquitin ligases, which regulate diverse cellular processes by targeting various substrates for degradation. However, the in vivo physiological function of RBX1 remains uncharacterized. Here, we show that a gene trap disruption of mouse Rbx1 causes embryonic lethality at embryonic day (E)7.5, mainly due to a failure in proliferation; p27, a cyclin dependent kinase inhibitor, normally undetectable in the early embryos, accumulates at high levels in the absence of Rbx1. Although mice heterozygous for the Rbx1 gene trap appear viable and fertile without obvious abnormalities, the Rbx1(+/Gt) MEFs do show retarded growth with G1 arrest and p27 accumulation. Simultaneous loss of p27 extended the life span of Rbx1(Gt/Gt) embryos from E6.5 to E9.5, indicating that p27-mediated cell cycle inhibition contributes to the early embryonic lethality in the Rbx1-deficient embryos. Our study demonstrates that the in vivo physiological function of RBX1 is to ensure cell proliferation by preventing p27 accumulation during the early stage of embryonic development.

Indexed as

AnimalsCarrier ProteinsCell LineCell ProliferationCyclin-Dependent Kinase Inhibitor p27Embryo LossEmbryo, MammalianEmbryonic Stem CellsFemaleGene Expression Regulation, DevelopmentalGenomeMaleMiceMice, TransgenicMutationTime FactorsCarrier ProteinsCyclin-Dependent Kinase Inhibitor p27RBX1 protein, mouse

Identifiers

PMID19325126
PMCPMC2669381
OpenAlexW2013171128

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.